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Updated: Jul 15, 2026

Crystal Structure of the N-terminal Domain of Ryanodine Receptor from Plutella xylostella
Published on: November 30, 2018
Expression, crystallization and preliminary crystallographic data analysis of filamin A repeats 14-16
Adeleke Halilu Aguda1, Amos Malle Sakwe, Lars Rask
1Department of Medical Biochemistry and Microbiology, Uppsala University, Sweden. adelekeha@imcb.a-star.edu.sg
Abstract:
Human filamin A is a 280 kDa protein involved in actin-filament cross-linking. It is structurally divided into an actin-binding headpiece (ABD) and a rod domain containing 24 immunoglobulin-like (Ig) repeats. A fragment of human filamin A (Ig repeats 14-16) was cloned and expressed in Escherichia coli and the purified protein was crystallized in 1.6 M ammonium sulfate, 2% PEG 1000 and 100 mM HEPES pH 7.5. The crystals diffracted to 1.95 A and belong to space group P2(1)2(1)2(1), with unit-cell parameters a = 50.63, b = 52.10, c = 98.46 A, alpha = beta = gamma = 90 degrees.
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